Parthenolide phosphorylation

Stimulation of macrophages by lipopolysaccharide (LPS) results in activation of members of MAPKs, ERKl and ERK2. The main sesquiterpene lactone from Tanacetum parthenium (Asteraceae), parthenolide (28), suppressed LPS-stimulated tyrosine phosphorylation of various proteins in RAW 264.7 cells. Of these proteins the MAPKs exhibited the most dramatic inhibition in response to parthenolide. 

Tyrosine phosphorylation of three MAPK subgroups (ERKl, ERK2 and P38) stimulated by LPS was inhibited by 28 in a dose dependent manner. It has been proposed that tyrosine kinase inhibition may occur through conjugation between the a-methylenebutyrolactone in parthenolide and the -SH group of target proteins [85]. 

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